Proteomics

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Spatiotemporally direct capturing global substrates of post-translational modifying enzymes in living cells

ABSTRACT: Methods for direct capturing global substrates of protein-modifying enzymes in living cells are with many challenges, and yet largely unexplored. Here, we report a strategy to directly capture substrates of protein-modifying enzymes via PTM-acceptor residue crosslinking in living cells, enabling global profiling of substrates of PTM-enzymes and validation of PTM-sites in a straightforward manner.

ORGANISM(S): Escherichia Coli

SUBMITTER: Minjia Tan  

PROVIDER: PXD040318 | iProX | Wed Feb 22 00:00:00 GMT 2023

REPOSITORIES: iProX

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Spatiotemporal and direct capturing global substrates of lysine-modifying enzymes in living cells.

Hu Hao H   Hu Wei W   Guo An-Di AD   Zhai Linhui L   Ma Song S   Nie Hui-Jun HJ   Zhou Bin-Shan BS   Liu Tianxian T   Jia Xinglong X   Liu Xing X   Yao Xuebiao X   Tan Minjia M   Chen Xiao-Hua XH  

Nature communications 20240217 1

Protein-modifying enzymes regulate the dynamics of myriad post-translational modification (PTM) substrates. Precise characterization of enzyme-substrate associations is essential for the molecular basis of cellular function and phenotype. Methods for direct capturing global substrates of protein-modifying enzymes in living cells are with many challenges, and yet largely unexplored. Here, we report a strategy to directly capture substrates of lysine-modifying enzymes via PTM-acceptor residue cros  ...[more]

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